The immunoreactive profile at the N-terminal region of A beta 1-39/40 but not A beta 1-42 changes with transition from monomer dimer to further peptide aggregates

被引:14
作者
Kametani, F [1 ]
Tanaka, K [1 ]
Tokuda, T [1 ]
Allsop, D [1 ]
机构
[1] SMITHKLINE BEECHAM PHARMACEUT,MOLEC NEUROPATHOL RES,HARLOW CM19 5AW,ESSEX,ENGLAND
关键词
A beta; amyloid; Alzheimer's disease; synthetic peptide; antibody; conformation;
D O I
10.1016/0006-8993(95)01195-1
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Using site-specific antibodies, we assessed the effect of aggregation of various length forms of A beta on the immunoreactive profile of the peptides. All of the antibodies tested reacted with monomeric/dimeric forms of A beta 1-42 and its further aggregates. However, antibodies directed against the 1-24 region of A beta reacted weakly or not at all with A beta 1-39/40 monomers or dimers, but immunoreactivity was enhanced substantially following peptide incubation and aggregation. These results suggest that the conformation of the N-terminal region of monomeric and dimeric A beta 1-39/40 is different from that of aggregated forms, whereas the longer AP 1-42 does not significantly change its N-terminal conformation during beta-sheet fibril formation. These immunochemical results are consistent with previous structural data, and help to explain the differential effects of A beta 1-39/40 and 1-42 on fibril formation in brain.
引用
收藏
页码:237 / 241
页数:5
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